4C31: Nup1:Sac3:Sus1 complex
Nup1:Sac3:Sus1 complex. Determined by X-ray diffraction at 3.0 Å resolution. Released 16 Apr 2014.
- Method
- X-ray diffraction
- Resolution
- 3.0 Å
- Organism
- SACCHAROMYCES CEREVISIAE
- Chains
- 8
- Atoms
- 2,340
- Mol. weight
- 45.86 kDa
- Released
- 16 Apr 2014
Explore 4C31 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4C31 contains 13 α-helices and 6 β-strands across 8 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chains A and D: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 757-784 | 28 | |
Chain B: 5 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-18 | 14 | |
| α-helix | 21-35 | 15 | |
| α-helix | 38-52 | 15 | |
| α-helix | 58-71 | 14 | |
| α-helix | 75-92 | 18 | |
| β-strand | 93 | 1 | 1 |
Chain C: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 331-332 | 2 | |
| β-strand | 333 | 1 | 2 |
Chain E: 5 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-18 | 14 | |
| α-helix | 21-35 | 15 | |
| α-helix | 38-52 | 15 | |
| α-helix | 58-72 | 15 | |
| α-helix | 75-92 | 18 | |
| β-strand | 93 | 1 | 3 |
Chain F: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 333 | 1 | 2 |
Chains X and Y: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 329 | 1 | 1 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Nuclear mRNA export protein SAC3 | A, D | protein | 33 | SACCHAROMYCES CEREVISIAE | P46674 (AlphaFold model) |
| Protein SUS1 | B, E | protein | 96 | SACCHAROMYCES CEREVISIAE | Q6WNK7 (AlphaFold model) |
| Nucleoporin NUP1 | C, F, X, Y | protein | 36 | SACCHAROMYCES CEREVISIAE | P20676 (AlphaFold model) |
Sequence of entity 1 (A, D), FASTA
>4C31_1 NUCLEAR MRNA EXPORT PROTEIN SAC3 (chains A, D)
GSRKDFIDTMTRELYDAFLHERLYLIYMDSRAE
Sequence of entity 2 (B, E), FASTA
>4C31_2 PROTEIN SUS1 (chains B, E)
MTMDTAQLKSQIQQYLVESGNYELISNELKARLLQEGWVDKVKDLTKSEMNINESTNFTQ
ILSTVEPKALEMVSDSTRETVLKQIREFLEEIVDTQ
Sequence of entity 3 (C, F, X, Y), FASTA
>4C31_3 NUCLEOPORIN NUP1 (chains C, F, X, Y)
GSPKKDKESIVLPTVGFDFIKDNETPSKKTSPKATS
Primary citation
Structural Basis for Binding the Trex2 Complex to Nuclear Pores, Gal1 Localisation and Mrna Export. Jani, D., Valkov, E., Stewart, M. Nucleic Acids Res (2014) 42:6686. DOI 10.1093/NAR/GKU252 · PubMed
Other PDB entries of the same protein (UniProt P46674 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8U8C 2.4 Å, Crystal structure of the TREX-2 complex in complex with the N-terminal motif of Sub2
- 3FWB 2.5 Å, Sac3:Sus1:Cdc31 complex
- 4MBE 2.61 Å, Sac3:Sus1:Cdc31:Nup1 complex
- 3FWC 2.7 Å, Sac3:Sus1:Cdc31 complex
- 3T5V 2.9 Å, Sac3:Thp1:Sem1 complex
- 8U8D 3.04 Å, Cryo-EM structure of the TREX-2 complex in complex with the N-terminal motif of Sub2
- 4TRQ 3.1 Å, Crystal structure of Sac3/Thp1/Sem1
- 8U8E 3.33 Å, Cryo-EM structure of the TREX-2 complex in association with Sub2
- 5L3T 4.93 Å, Structure of the Saccharomyces cerevisiae TREX-2 complex
- 5G5P 5.3 Å, Structure of the Saccharomyces cerevisiae TREX-2 complex
Browse structure collections
About this viewer
MolViewer shows 4C31 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.